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作 者:Jianwei Lin Xiang David Li
机构地区:[1]Department of Chemistry,The University of Hong Kong
出 处:《Chinese Chemical Letters》2018年第7期1051-1057,共7页中国化学快报(英文版)
基 金:support from the Hong Kong Research Grants Council Collaborative Research Fund(CRF No. C7029-15G);the Areas of Excellence Scheme (No. AoE/P-705/16);the General Research Fund (GRF Nos.17125917 and 17303114);the Early CareerScheme(ECS)(HKU No. 709813P);the National Natural Science Foundation of China(Nos. 21572191 and 91753130)
摘 要:Increasing amount of evidence suggests that post-translational modifications(PTMs) on histones are involved in regulating DNA-associated processes such as gene expression and DNA-damage repair. To identify and characterize proteins that recognize histone PTMs, tools relying on synthetic peptides have been constructed and widely used in recent years. In this review, we first summarize the development and applications of these tools, which includes peptide-based pull-down assay and peptide-array-based high-throughput screening. The limitation of peptide-based approaches is then discussed, followed by a brief description on recent development of nucleosome-based tools.Increasing amount of evidence suggests that post-translational modifications(PTMs) on histones are involved in regulating DNA-associated processes such as gene expression and DNA-damage repair. To identify and characterize proteins that recognize histone PTMs, tools relying on synthetic peptides have been constructed and widely used in recent years. In this review, we first summarize the development and applications of these tools, which includes peptide-based pull-down assay and peptide-array-based high-throughput screening. The limitation of peptide-based approaches is then discussed, followed by a brief description on recent development of nucleosome-based tools.
关 键 词:Histone PTMs Peptide pull-down Crosslinkers Peptide microarrays Peptide libraries
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